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Home / Primary Antibodies / Polyclonal Antibodies

HSP90 (Salmon) Antibody - SPC-316

BHA11907727
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Email
[email protected]
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Swissprot Q9W6K6
Accession Number NP_001117004.1
Gene Id 100136360
Target HSP90
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Tumor Biomarkers, Protein Trafficking
Buffer Lyophilized rabbit Antiserum. For reconstitution add 100 µl of sterile water.
Dilutions WB (1:5000); optimal dilutions for assays should be determined by the user.
Purification Rabbit Antiserum
Scientific Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer.(2) From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling. (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5 When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.
In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). Looking for more information on HSP90 Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Shipping Temperature Blue Ice or 4°C
Specificity Detects ~90kDa. In salmonid fish a cross-reactive band at 40kDa is observed. Antibody will also detect a Human recombinant HSP90 protein.
Storage -20ºC
Storage Buffer Lyophilized rabbit Antiserum. For reconstitution add 100 ul of sterile water.
Storage Temperature -20°C
Applications WB
Description WB
Dilution WB (1:5000); optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 1. Nemoto T., et al. (1997) J.Biol Chem. 272: 26179-26187.

2. Minami Y., et al. (1991), J.Biol Chem. 266: 10099-10103.

3. Arlander S.J.H., et al. (2003) J Biol Chem 278: 52572-52577.

4. Pearl H., et al. (2001) Adv Protein Chem 59:157-186.

5. Neckers L., et al. (2002) Trends Mol Med 8:S55-S61.

6. Pratt W., Toft D. (2003) Exp Biol Med 228:111-133.

7. Pratt W., Toft D. (1997) Endocr Rev 18:306–360.

8. Pratt W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434.

9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.

10. Barent R. L. (1998) Mol. Endocrinol. 12: 342-354

11. Lo. M.A. (1998) EMBO J. 17: 6879-6887.
Combination SKU Supplier No. Conjugate Size Your price Quantity
BHA11907727-1 SPC-316D Unconjugated 100 ul $345
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